epitope mapping near the C-terminus of FAAH of human origin
recommended for detection of fatty acid amide hydrolase of mouse, rat and human origin by WB, IF and ELISA; also reactive with additional species, including equine, canine, bovine, porcine and avian
FAAH Background Information FAAH is a membrane-bound enzyme fatty acid amide hydrolase, responsible for the hydrolysis of multiple primary and secondary fatty acid amides, including the neuromodulatory compounds anandamine and oleamide (1). The degradation of anandamide to arachadonic acid and oleamide to oleic acid, terminates the signaling function of these molecules (2, 3). FAAH degrades amides and esters with equivalent catalytic efficiency, enabling FAAH to function effectively as both an amidase and esterase (4). FAAH contributes to anandamide uptake by creating and maintaining an inward concentration gradient for anandamide (5). A natural single nucleotide polymorphism mutation in human FAAH in its homozygous form is strongly associated with problem drug use (6). This results in a missense mutation (385C-->A) that converts a conserved proline residue to threonine (Pro129-->Thr), producing an FAAH variant that displays normal catalytic properties but enhanced sensitivity to proteolytic degradation (6). Genetic mutations in FAAH consitute an important risk factor for problem drug use (6). The human FAAH gene maps to chromosome 1p33 (7).
